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. 2020 Sep 1;9:e58675. doi: 10.7554/eLife.58675

Figure 6. V24 of H3t is an optimal residue for the H3t recognition by the Tudor domain of PHF1/19.

Figure 6.

(A) Binding affinities of PHF1 and PHF19 Tudor domain with various peptides determined using ITC. (B) The crystal structure of PHF1 in complex with H3K36me3H39V. The mutant H3K36me3H39V peptide is shown as a stick in light magenta. PHF1 is shown as surface and the hydrophobic patch surrounding V39 is indicated in cyan. Some additional interactions in the H3K36me3-H39V mutant are indicated with dash lines. (C) Structural comparison of PHF1-H3K36me3 (PDB: 4HCZ) and PHF1-H3K36me3-H39V. The four leucines involved in hydrophobic interactions are shown with stick in cyan. The H3K36me3 peptide and H3K36me3-H39V mutant are shown as cartoon in pale green and light magenta, respectively. (D) The sequence alignment of H3t from human, mouse, and rat. The secondary structure elements are shown above the sequence. Identical residues are indicated in aqua and the different residues are colored in red.